1rlr
From Proteopedia
(New page: 200px<br /><applet load="1rlr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlr, resolution 2.5Å" /> '''STRUCTURE OF RIBONUCL...) |
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| - | [[Image:1rlr.jpg|left|200px]]<br /><applet load="1rlr" size=" | + | [[Image:1rlr.jpg|left|200px]]<br /><applet load="1rlr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rlr, resolution 2.5Å" /> | caption="1rlr, resolution 2.5Å" /> | ||
'''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1'''<br /> | '''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ribonucleotide reductase is the only enzyme that catalyses de novo | + | Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1RLR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Full crystallographic information is available from [http:// | + | 1RLR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: reductase (acting on ch2)]] | [[Category: reductase (acting on ch2)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:15 2008'' |
Revision as of 12:52, 21 February 2008
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STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1
Overview
Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction.
About this Structure
1RLR is a Single protein structure of sequence from Escherichia coli. Active as Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 Full crystallographic information is available from OCA.
Reference
Structure of ribonucleotide reductase protein R1., Uhlin U, Eklund H, Nature. 1994 Aug 18;370(6490):533-9. PMID:8052308
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